Anti-citrullinated α-Enolase antibody
Description
Application Data
Description
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Recognises α-enolase with a citrullinated arginine residue, a key target for auto-antibodies in rheumatoid arthritis
Application Data
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Alpha-enolase is an evolutionary conserved, multifunctional protein, best known for its role in glucose metabolism, and as a plasminogen-binding protein on the surface of various mammalian and prokaryotic cell types. Citrullinated α-enolase is one of the key targets for auto-antibodies in rheumatoid arthritis (RA) and such antibodies can be found in 40–60% of patients with RA. Citrullination is a post-translational modification of arginine residues, mediated by the family of peptidylarginine deiminases (PAD).
Alpha-enolase is an evolutionary conserved, multifunctional protein, best known for its role in glucose metabolism, and as a plasminogen-binding protein on the surface of various mammalian and prokaryotic cell types. Citrullinated α-enolase is one of the key targets for auto-antibodies in rheumatoid arthritis (RA) and such antibodies can be found in 40–60% of patients with RA. Citrullination is a post-translational modification of arginine residues, mediated by the family of peptidylarginine deiminases (PAD).
| Catalogue number | crb2005010 |
|---|---|
| Antibody | Anti-citrullinated α-Enolase antibody |
| Antigen Peptide | KLH conjugated synthetic peptide crb1200290e |
| Protein ID | UniProtKB - P06733 |
| Cross-Reactivity | Human, rat, chicken |
| Host Species | Rabbit |
| Antibody Type | Polyclonal |
| Label | Unconjugated |
| Concentration | 1mg/ml |
| Validation | WB/ELISA |
| Target | citrullinated α-Enolase |
| Disease Area | Autoimmune |
| Specificity | Citrullinated form |
| Post-translational Modification | Citrullination |
| Citations | Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K., Lundberg, K., Kinloch, A., Culshaw, S., Potempa, J. and Venables, P. (2010). Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and α-enolase: Implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum, 62(9), 2662-2672. PMID: 20506214
Wegner, N., Wait, R. and Venables, P. (2009). Evolutionarily conserved antigens in autoimmune disease: Implications for an infective aetiology. Int J Biochem Cell Biol, 41(2), 390-397. PMID: 18926919 |
| References | Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K., Lundberg, K., Kinloch, A., Culshaw, S., Potempa, J. and Venables, P. (2010). Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and α-enolase: Implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum, 62(9), 2662-2672. PMID: 20506214
Wegner, N., Wait, R. and Venables, P. (2009). Evolutionarily conserved antigens in autoimmune disease: Implications for an infective aetiology. Int J Biochem Cell Biol, 41(2), 390-397. PMID: 18926919 |
Alpha-enolase is an evolutionary conserved, multifunctional protein, best known for its role in glucose metabolism, and as a plasminogen-binding protein on the surface of various mammalian and prokaryotic cell types. Citrullinated α-enolase is one of the key targets for auto-antibodies in rheumatoid arthritis (RA) and such antibodies can be found in 40–60% of patients with RA. Citrullination is a post-translational modification of arginine residues, mediated by the family of peptidylarginine deiminases (PAD).